Purification and characterization of two endopolygalacturonases secreted during the early stages of the saprophytic growth of Sclerotinia sclerotiorum.
Two endopolygalacturonases (endo-PGs) secreted at the early stage of cultures of Sclerotinia sclerotiorum grown on polygalacturonate medium, were purified to apparent homogeneity, using ion exchange chromatography. They are glycoproteins of an apparent weight of 42 and 41.5 kDa and a pI of 4.8. The two purified isoforms found in early cultures were not detected in late cultures. Purification of the isoforms secreted at different stages of growth revealed that the increase of polygalacturonase activity during the culture corresponds to a sequential production of enzymes and to the successive replacement of isoforms by new enzymes.
Martel
M B
MB
Centre de Génétique Moléculaire et Cellulaire, UMR-CNRS 5534, Université Lyon I (Bât, 405), Villeurbanne, France.
Létoublon
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Fèvre
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M
D001203:Ascomycota / Q000201:enzymology* / Q000254:growth & development; D003470:Culture Media; D004591:Electrophoresis, Polyacrylamide Gel; D007527:Isoenzymes / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D010368:Pectins; D011096:Polygalacturonase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*
D003470:Culture Media; D007527:Isoenzymes; D010368:Pectins; D011096:Polygalacturonase; C003181:polygalacturonic acid